Dissecting the assembly pathway of the 20S proteasome

FEBS Lett. 1997 Nov 24;418(1-2):189-94. doi: 10.1016/s0014-5793(97)01370-7.

Abstract

Proteasomes reach their mature active state via a complex cascade of folding, assembly and processing events. The Rhodococcus proteasome offers a means to dissect the assembly pathway and to characterize intermediates; its four subunits (alpha1, alpha2, beta1, beta2) assemble efficiently in vitro with any combination of alpha and beta. Assembly studies with wild-type and N-terminally truncated beta-subunits in conjunction with refolding studies allowed to define the role of the propeptide which is two-fold: It supports the initial folding of the beta-subunits and it promotes the maturation of the holoproteasomes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Cysteine Endopeptidases / biosynthesis*
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / ultrastructure
  • Enzyme Precursors / chemistry
  • Kinetics
  • Macromolecular Substances
  • Microscopy, Electron
  • Models, Molecular
  • Multienzyme Complexes / biosynthesis*
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / ultrastructure
  • Polymerase Chain Reaction
  • Proteasome Endopeptidase Complex
  • Protein Conformation*
  • Protein Denaturation
  • Protein Folding*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Rhodococcus / enzymology*
  • Sequence Tagged Sites
  • Substrate Specificity

Substances

  • Enzyme Precursors
  • Macromolecular Substances
  • Multienzyme Complexes
  • Recombinant Proteins
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex